Reviewed,
UniProtKB/Swiss-Prot P22534 (GUNA_CALSA)
Last modified
May 5, 2009.
Version 71.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Endoglucanase A EC=3.2.1.4 Alternative name(s): Endo-1,4-beta-glucanase A Cellulase A | ||
| Gene names |
| ||
| Organism | Caldocellum saccharolyticum (Caldicellulosiruptor saccharolyticus) | ||
| Taxonomic identifier | 44001 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor |
Protein attributes
| Sequence length | 1742 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | The N-terminal domain of celA encodes for an endoglucanase activity on carboxymethylcellulose. The C-terminal domain probably acts synergistically to hydrolyze crystalline cellulose. |
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| Post-translational modification | The linker region (also termed "hinge") may be a potential site for proteolysis. |
| Sequence similarities | In the N-terminal section; belongs to the glycosyl hydrolase 9 (cellulase E) family. In the C-terminal section; belongs to the glycosyl hydrolase 48 (cellulase L) family. Contains 3 CBM3 (carbohydrate binding type-3) domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Domain | Repeat Signal |
| Molecular function | Glycosidase Hydrolase |
| Gene Ontology (GO) | |
| Biological process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | carbohydrate binding Inferred from electronic annotation. Source: InterPro cellulase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | ||||||
| Chain | 24 – 1742 | 1719 | Endoglucanase A | PRO_0000007944 | |||||
Regions | |||||||||
| Domain | 477 – 637 | 161 | CBM3 1 | ||||||
| Domain | 703 – 856 | 154 | CBM3 2 | ||||||
| Domain | 906 – 1059 | 154 | CBM3 3 | ||||||
| Region | 24 – 476 | 453 | Catalytic 1 | ||||||
| Region | 638 – 702 | 65 | Linker ("hinge") (Pro-Thr box) | ||||||
| Region | 857 – 905 | 49 | Linker ("hinge") (Pro-Thr box) | ||||||
| Region | 1060 – 1112 | 53 | Linker ("hinge") (Pro-Thr box) | ||||||
| Region | 1113 – 1742 | 630 | Catalytic 2 | ||||||
Sites | |||||||||
| Active site | 396 | 1 | By similarity | ||||||
| Active site | 434 | 1 | By similarity | ||||||
| Active site | 443 | 1 | By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 1545 | 1 | T → A in AAA72860. Ref.2 | ||||||
Sequences
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References
| [1] | "celA, another gene coding for a multidomain cellulase from the extreme thermophile Caldocellum saccharolyticum." Te'O V.S. Jr., Saul D.J., Bergquist P.L. Appl. Microbiol. Biotechnol. 43:291-296(1995) [PubMed: 7612247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a beta-mannanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum'." Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L. Appl. Environ. Microbiol. 57:694-700(1991) [PubMed: 2039230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1516-1742. |
Cross-references
Sequence databases | |
|---|---|
| L32742 Genomic DNA. Translation: AAA91086.1. M36063 Genomic DNA. Translation: AAA72860.1. L01257 Unassigned DNA. No translation available. | |
| PIR | T17120. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1G87 based on UniProtKB P37700. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM3. Carbohydrate-Binding Module Family 3. GH48. Glycoside Hydrolase Family 48. GH9. Glycoside Hydrolase Family 9. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.4. 15230. |
Family and domain databases | |
| InterPro | IPR012341. 6hp_glycosidase. IPR001956. CBD_3. IPR000556. Glyco_hydro_48F. IPR001701. Glyco_hydro_9. IPR018221. Glyco_hydro_9_AS. [Graphical view] |
| Gene3D | G3DSA:2.60.40.710. CBD_3. 1 hit. G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit. |
| PANTHER | PTHR22298:SF3. Glyco_hydro_9. 1 hit. |
| Pfam | PF00942. CBM_3. 3 hits. PF02011. Glyco_hydro_48. 1 hit. PF00759. Glyco_hydro_9. 1 hit. [Graphical view] |
| PRINTS | PR00844. GLHYDRLASE48. |
| ProDom | PD001947. CBD_3. 3 hits. PD011903. Glyco_hydro_48. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS51172. CBM3. 3 hits. PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit. PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GUNA_CALSA | ||||||||
| Accession | Primary (citable) accession number: P22534 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |
